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1.2.1.89: D-glyceraldehyde dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about D-glyceraldehyde dehydrogenase (NADP+), go to the full flat file.

Word Map on EC 1.2.1.89

Reaction

D-glyceraldehyde
+
NADP+
+
H2O
=
D-glycerate
+
NADPH
+
H+

Synonyms

AldA, ALDH, GADH, GLD, glyceraldehyde dehydrogenase, Pto0332, Ta0809, TaAlDH

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.89 D-glyceraldehyde dehydrogenase (NADP+)

Engineering

Engineering on EC 1.2.1.89 - D-glyceraldehyde dehydrogenase (NADP+)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N286E
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286H
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286T
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
34M/Y399C/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 55.7
F34L
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 3.2
F34M/D372N/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 7.2
F34M/D372N/Y399C/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 35.1
F34M/S405N
F34M/W271R/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 22.6
F34M/W271S/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 42.5
F34M/W271S/Y399C/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 1.1
F34M/Y399C/S405N
enhances enzyme activity with the cofactor NAD+ by a factor of eight and enhances solubilty
S405C
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 6
S405N
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 7.4
W271S
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 17.1
Y399C
F34M/S405N
-
the mutant shows a slight increase in NAD+ acceptance and a 9fold improvement in catalytic efficiency with NAD+ compared with the wild type enzyme
-